Dataset Information

Production and purification of laccase by Bacillus sp. using millet husks and its pesticide degradation application.

ABSTRACT: Lignocellulosic agricultural bi-products, pearl millet (PM) and finger millet (FM) husks, were used for the production of laccase using Bacillus sp. PS under solid-state fermentation (SSF). Abiotic variables such as substrate (PM, FM) concentration (1-5%), incubation time (24-96 h) and pH (5-10) were optimized using Response surface methodology (RSM) to maximize the laccase production. The predicted model showed maximum laccase activity of 402 U/mL appearing after 96 h of incubation with PM 2.0 g/L and FM 1.5 g/L at pH 7.0. Single protein band on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) confirmed homogeneity of the laccase with a molecular weight of 63-75 kDa. The partially purified laccase effectively degraded the pesticides (Tricel, 71.8?±?3.5 and Phoskill 77.3?±?3.4%) within 5 days of incubation (40 °C) in pH 7.0. The pesticide degradation was further confirmed by high-performance liquid chromatography (HPLC) and the chromatograms showed the single dominant peaks at retention time 2.482 (tricel) and 2.608 (phoskill) min, respectively. Pesticide-degrading laccase was produced by Bacillus sp. PS under SSF reveals the utilization of low-cost bi-substrates for enhanced laccase production.

SUBMITTER: Srinivasan P

PROVIDER: S-EPMC6789060 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

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Production and purification of laccase by <i>Bacillus</i> sp. using millet husks and its pesticide degradation application.

Srinivasan P P Selvankumar T T Kamala-Kannan S S Mythili R R Sengottaiyan A A Govarthanan M M Senthilkumar B B Selvam K K

3 Biotech 20191011 11

Lignocellulosic agricultural bi-products, pearl millet (PM) and finger millet (FM) husks, were used for the production of laccase using <i>Bacillus</i> sp. PS under solid-state fermentation (SSF). Abiotic variables such as substrate (PM, FM) concentration (1-5%), incubation time (24-96 h) and pH (5-10) were optimized using Response surface methodology (RSM) to maximize the laccase production. The predicted model showed maximum laccase activity of 402 U/mL appearing after 96 h of incubation with ...[more]

PMID: 31656734

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Project description:For the enzymatic production of chitosan oligosaccharides from chitosan, a chitosanase-producing bacterium, Bacillus sp. strain KCTC 0377BP, was isolated from soil. The bacterium constitutively produced chitosanase in a culture medium without chitosan as an inducer. The production of chitosanase was increased from 1.2 U/ml in a minimal chitosan medium to 100 U/ml by optimizing the culture conditions. The chitosanase was purified from a culture supernatant by using CM-Toyopearl column chromatography and a Superose 12HR column for fast-performance liquid chromatography and was characterized according to its enzyme properties. The molecular mass of the enzyme was estimated to be 45 kDa by means of sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme demonstrated bifunctional chitosanase-glucanase activities, although it showed very low glucanase activity, with less than 3% of the chitosanase activity. Activity of the enzyme increased with an increase of the degrees of deacetylation (DDA) of the chitosan substrate. However, the enzyme still retained 72% of its relative activity toward the 39% DDA of chitosan, compared with the activity of the 94% DDA of chitosan. The enzyme produced chitosan oligosaccharides from chitosan, ranging mainly from chitotriose to chitooctaose. By controlling the reaction time and by monitoring the reaction products with gel filtration high-performance liquid chromatography, chitosan oligosaccharides with a desired oligosaccharide content and composition were obtained. In addition, the enzyme was efficiently used for the production of low-molecular-weight chitosan and highly acetylated chitosan oligosaccharides. A gene (csn45) encoding chitosanase was cloned, sequenced, and compared with other functionally related genes. The deduced amino acid sequence of csn45 was dissimilar to those of the classical chitosanase belonging to glycoside hydrolase family 46 but was similar to glucanases classified with glycoside hydrolase family 8.

Dataset Information

Production and purification of laccase by Bacillus sp. using millet husks and its pesticide degradation application.

Publications

Production and purification of laccase by <i>Bacillus</i> sp. using millet husks and its pesticide degradation application.

Similar Datasets

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